Reactivity | MuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind biotinylated Pam3CysSerLys4 (Pam3CSK4). |
Source | Mouse myeloma cell line, NS0-derived mouse TLR1 protein Ser25-Asp581, with a C-terminal 10-His tag |
Accession # | |
N-terminal Sequence | Ser25 |
Protein/Peptide Type | Recombinant Proteins |
Gene | Tlr1 |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 64.2 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE | 85-95 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
The Toll-like family of molecules are type I transmembrane proteins that serve as pattern recognition receptors for microbial pathogens. There are at least twelve mouse and ten human TLRs that activate the innate immune system following exposure to a variety of microbial species (1, 2). TLRs contain a large number of leucine-rich repeats (LRRs) and a cytoplasmic tail with one Toll/IL-1 receptor (TIR) domain. Mature mouse TLR1 consists of a 557 amino acid (aa) extracellular domain (ECD) with 20 LRRs, a 21 aa transmembrane segment, and a 192 aa cytoplasmic domain (3, 4). Within the ECD, mouse TLR1 shares 60% aa sequence identity with mouse TLR6 and 19% -27% aa sequence identitity with mouse TLR2, -3, -4, -5, -7, -8, -9, -11, -12, and -13. It shares 73% and 86% aa sequence identity with human and rat TLR1, respectively. TLR1 is expressed on the surface of macrophages, dendritic cells, and tonsillar epithelial cells in ligand-independent association with TLR2 (5 - 8). TLR2 additionally associates with TLR6 to form a functional complex with specificity for distinct but related microbial ligands (9 - 11). TLR1 and TLR2 cooperate in the recognition of bacterial and protozoal triacylated lipopeptides and glycosylphosphatidylinositols (6, 10 - 12). Ligand binding induces TLR1 localization to lipid rafts followed by receptor internalization and activation of NF kappa B (7, 11, 13).
Toll-like receptor 2 activation contributes to oral squamous cell carcinoma development and miRNA-mediated drug resistance By Jamshed Arslan, Pharm. D., PhD. Squamous cell carcinoma is the most common cancer in the oral cavity.1 The tumor surface biofilms in oral cancers contain high levels of aerobic and anaerobic microorganisms.1,2 Peri... Read full blog post. |
The role of STING/TMEM173 in gamma and encephalitis Herpes Simplex Virus (HSV) Stimulator of interferon genes (STING), also known as TMEM173, promotes the production of the interferon’s IFN-alpha and IFN-beta. STING possesses three functional domains: a cytoplasmic C-terminal tail, a central globular domain, and four N-... Read full blog post. |
TLR1 TLR1 belongs to the Toll-like receptor (TLR) family, and is a key player in the recognition of pathogens as well as the activation of the innate immunity system. TLRs are highly conserved proteins with a high degree of structural and functional homolo... Read full blog post. |
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